Recombinant DNA Approaches to the Study of the Regulation of Virulence Factors and Epidemiology of Pseudomonas aeruginosa1

2015 ◽  
pp. 264-278 ◽  
Author(s):  
Michael L. Vasil ◽  
John W. Ogle ◽  
Christopher C. R. Grant ◽  
Adriana L. Vasil
Keyword(s):  
Virulence Factors ◽  
Recombinant Dna

mRNA localization by Electron microscopic in situ hybridization

1991 ◽  
Vol 49 ◽  
pp. 430-431
Author(s):  
J. A. Pollock ◽  
M. Martone ◽  
T. Deerinck ◽  
M. H. Ellisman
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Nucleic Acids ◽  
Recombinant Dna ◽  
Light And Electron Microscopy ◽  
Electron Microscopic ◽  
High Voltage Electron Microscopy ◽  
Functional Sites ◽  
Voltage Electron

Localization of specific proteins in cells by both light and electron microscopy has been facilitate by the availability of antibodies that recognize unique features of these proteins. High resolution localization studies conducted over the last 25 years have allowed biologists to study the synthesis, translocation and ultimate functional sites for many important classes of proteins. Recently, recombinant DNA techniques in molecular biology have allowed the production of specific probes for localization of nucleic acids by “in situ” hybridization. The availability of these probes potentially opens a new set of questions to experimental investigation regarding the subcellular distribution of specific DNA's and RNA's. Nucleic acids have a much lower “copy number” per cell than a typical protein, ranging from one copy to perhaps several thousand. Therefore, sensitive, high resolution techniques are required. There are several reasons why Intermediate Voltage Electron Microscopy (IVEM) and High Voltage Electron Microscopy (HVEM) are most useful for localization of nucleic acids in situ.

Immunogold labeling of CMP-KDO synthetase produced by recombinant E. Coli cells

1987 ◽  
Vol 45 ◽  
pp. 924-925
Author(s):  
F. A. Durum ◽  
R. G. Goldman ◽  
T. J. Bolling ◽  
M. F. Miller
Keyword(s):  
Inclusion Bodies ◽  
Large Scale ◽  
Recombinant Dna ◽  
Test System ◽  
Cell Protein ◽  
Gram Negative Bacteria ◽  
Cytoplasmic Inclusions ◽  
Isolation And Purification ◽  
E Coli ◽  
Low Concentrations

CMP-KDO synthetase (CKS) is an enzyme which plays a key role in the synthesis of LPS, an outer membrane component unique to gram negative bacteria. CKS activates KDO to CMP-KDO for incorporation into LPS. The enzyme is normally present in low concentrations (0.02% of total cell protein) which makes it difficult to perform large scale isolation and purification. Recently, the gene for CKS from E. coli was cloned and various recombinant DNA constructs overproducing CKS several thousandfold (unpublished data) were derived. Interestingly, no cytoplasmic inclusions of overproduced CKS were observed by EM (Fig. 1) which is in contrast to other reports of large proteinaceous inclusion bodies in various overproducing recombinant strains. The present immunocytochemical study was undertaken to localize CKS in these cells.Immune labeling conditions were first optimized using a previously described cell-free test system. Briefly, this involves soaking small blocks of polymerized bovine serum albumin in purified CKS antigen and subjecting them to various fixation, embedding and immunochemical conditions.

A Multicenter Study of Recombinant Factor VIII (RecombinateTM) in Previously Treated Patients with Hemophilia A

1997 ◽  
Vol 77 (04) ◽  
pp. 660-667 ◽  
Author(s):  
G C White ◽  
S Courter ◽  
G L Bray ◽  
M Lee ◽  
E D Gomperts ◽  
...  
Keyword(s):  
Hemophilia A ◽  
Recombinant Dna ◽  
Home Treatment ◽  
Pharmacokinetic Parameters ◽  
Pharmacokinetic Studies ◽  
Open Label ◽  
Treat Ment ◽  
Previously Treated Patients ◽  
Bleeding Episodes

SummaryA prospective, open-label multicenter investigation has been conducted to compare pharmacokinetic parameters of recombinant DNA-derived FVIII (rFVIII) and plasma-derived FVIII concentrate (pdFVIII) and to assess safety and efficacy of long-term home-treat- ment with rFVIII for subjects with hemophilia A. Following comparative in vivo pharmacokinetic studies, 69 patients with severe (n = 67) or moderate (n = 2) hemophilia A commenced a program of home treatment using rFVIII exclusively for prophylaxis and treatment of all bleeding episodes for a period of 1.0 to 5.7 years (median 3.7 years). The mean in vivo half-lives of rFVIII and pdFVIII were both 14.7 h. In vivo incremental recoveries at baseline were 2.40%/IU/kg and 2.47%/IU/kg, respectively (p = 0.59). The response to home treatment with rFVIII was categorized as good or excellent in 3,195 (91.2%) of 3,481 evaluated bleeding episodes. Thirteen patients received rFVIII for prophylaxis for twenty-four surgical procedures. In all cases, hemostasis was excellent. Adverse reactions were observed in only 13 of 13,591 (0.096%) infusions of rFVIII; none was serious. No patient developed an inhibitor to r FVIII.

Enterococcal Virulence Determinants In Urinary Tract Infection Patients

2012 ◽  
Vol 6 (1) ◽  
pp. 14-17
Author(s):  
Jabin Akhter ◽  
Shaheda Anwar ◽  
Sharmeen Ahmed
Keyword(s):  
Urinary Tract Infection ◽  
Urinary Tract ◽  
Tract Infection ◽  
Virulence Factors ◽  
Virulence Determinants ◽  
Microtitre Plate ◽  
Microbiological Method ◽  
Enterococcal Infection ◽  
Microtitre Plate Assay ◽  
Positive Frequency

Urinary tract infection caused by Enterococci has become frequent occurrences in health care settings. Currently they emerged with increasing resistance to multiple antibiotics.  Haemolysin, gelatinase and biofilm production are some markers that have been proposed as possible Enterococcal virulence factors. In view of the increasing importance of Enterococcal infection, the present study was designed to isolate and identify the Enterococci to the species level from urine of urinary tract infection patients and to investigate their possible virulence factors. Biofilm was detected on polystyrene microtitre plate to see the adherence of microorganism. Haemolysin production and gelatin hydrolysis detected by standard microbiological method. Fifty nine enterococcal isolates were speciated by conventional microbiological method and examined for their ability to form biofilm by microtitre plate assay. In this study, biofilm formations by Enterococci were found in 83.33% isolates from catheterized and 56.09% from non-catheterized patients. Aong them, E.faecalis & 50% E.faecium produced biofilm. About 43.63% E.faecalis & 10% E.faecium produced haemolysin and only one isolate were found to be gelatinase positive. Frequency of virulence factors (VFs) in combination was observed in this study. Two VFs (haemolysin and biofilm) were observed in 27.11% in combination and 3 VFs ( haemolysinm biofilm and gelatinase) were present in 1.69% isolates. These results suggest that although there may not be an absolute role for individual virulence determinants in infectivity, combinations of factors may play a role in allowing a biofilm infection to be more resistant to therapy.DOI: http://dx.doi.org/10.3329/bjmm.v6i1.19361 Bangladesh J Med Microbiol 2012; 06(01): 14-17

Microbiological characteristic bacteria of the genus Legionella: classification, morphology and physiology, virulence factors – part I

2014 ◽  
Vol 5 (1) ◽  
pp. 17-25
Author(s):  
Agnieszka Sikora ◽  
Małgorzata Wójtowicz-Bobin ◽  
Anna Sikora ◽  
Maria Kozioł-Montewka ◽  
Dagmara Strzelec - Nowak
Keyword(s):  
Virulence Factors

Investigation on bla Ctx-M-1 , Virulence Factors and Multidruge Resistance in Pseudomonas Aeruginosa Bacteria

2017 ◽  
Vol 13 (3) ◽  
pp. 206-221
Author(s):  
Hadi Rahman Rasheed Al-Taai ◽  
◽  
Zainab Mohammed Hameed ◽  
Izdehar Mohammed Jasim
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Virulence Factors

Evaluation of the antibiotic susceptibility and virulence factors production in Staphylococcus spp. strains used to obtain autologous vaccines

Infectio ro ◽  
2018 ◽  
Vol 2 (54) ◽  
pp. 27
Author(s):  
Mădălina Preda ◽  
Alina Maria Holban ◽  
Lia-Mara Diţu ◽  
Coralia Bleotu ◽  
Mădălina-Maria Muntean ◽  
...  
Keyword(s):  
Virulence Factors ◽  
Antibiotic Susceptibility ◽  
Staphylococcus Spp
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